Structural highlights
Function
VAMP2_RAT Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca(2+)-evoked neurotransmitter release. A combined X-ray and TROSY-based NMR study now reveals the atomic structure of the complexin/SNARE complex. Complexin binds in an antiparallel alpha-helical conformation to the groove between the synaptobrevin and syntaxin helices. This interaction stabilizes the interface between these two helices, which bears the repulsive forces between the apposed membranes. These results suggest that complexin stabilizes the fully assembled SNARE complex as a key step that enables the exquisitely high speed of Ca(2+)-evoked neurotransmitter release.
Three-dimensional structure of the complexin/SNARE complex.,Chen X, Tomchick DR, Kovrigin E, Arac D, Machius M, Sudhof TC, Rizo J Neuron. 2002 Jan 31;33(3):397-409. PMID:11832227[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen X, Tomchick DR, Kovrigin E, Arac D, Machius M, Sudhof TC, Rizo J. Three-dimensional structure of the complexin/SNARE complex. Neuron. 2002 Jan 31;33(3):397-409. PMID:11832227
